FAM86B2 protein (human) - STRING interaction network

Nodes:

Network nodes represent proteins

splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.

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query proteins and first shell of interactors

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second shell of interactors

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empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Knowledge-based Evidence

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textmining

Assay-based Predictions

experimentally determined

co-expression

Genomic Predictions

gene neighborhood

gene co-occurrence

gene fusions

Your Current Organism:

Homo sapiens

NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man

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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
C8orf48	DEFB130A	ENSP00000297324	ENSP00000382951	Uncharacterized protein C8orf48; Chromosome 8 open reading frame 48.	Beta-defensin 130A; Antimicrobial host-defense peptide. Has an antiplasmodial activity.	0.427
C8orf48	FAM86B2	ENSP00000297324	ENSP00000262365	Uncharacterized protein C8orf48; Chromosome 8 open reading frame 48.	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	0.470
CCT3	CCT4	ENSP00000295688	ENSP00000377958	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	T-complex protein 1 subunit delta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	0.999
CCT3	FAM86B2	ENSP00000295688	ENSP00000262365	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	0.467
CCT3	TUBB6	ENSP00000295688	ENSP00000318697	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	Tubulin beta-6 chain; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Belongs to the tubulin family.	0.750
CCT4	CCT3	ENSP00000377958	ENSP00000295688	T-complex protein 1 subunit delta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	0.999
CCT4	FAM86B2	ENSP00000377958	ENSP00000262365	T-complex protein 1 subunit delta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	0.535
CCT4	TUBB6	ENSP00000377958	ENSP00000318697	T-complex protein 1 subunit delta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	Tubulin beta-6 chain; Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain. Belongs to the tubulin family.	0.730
DEFB130A	C8orf48	ENSP00000382951	ENSP00000297324	Beta-defensin 130A; Antimicrobial host-defense peptide. Has an antiplasmodial activity.	Uncharacterized protein C8orf48; Chromosome 8 open reading frame 48.	0.427
DEFB130A	FAM86B2	ENSP00000382951	ENSP00000262365	Beta-defensin 130A; Antimicrobial host-defense peptide. Has an antiplasmodial activity.	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	0.494
EEF2KMT	FAM86B1	ENSP00000398502	ENSP00000407067	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'.	Putative protein N-methyltransferase FAM86B1; Family with sequence similarity 86 member B1.	0.924
EEF2KMT	FAM86B2	ENSP00000398502	ENSP00000262365	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'.	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	0.998
EEF2KMT	RFFL	ENSP00000398502	ENSP00000326170	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'.	E3 ubiquitin-protein ligase rififylin; E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. Negatively regulates the tumor ne [...]	0.943
FAM86B1	EEF2KMT	ENSP00000407067	ENSP00000398502	Putative protein N-methyltransferase FAM86B1; Family with sequence similarity 86 member B1.	Protein-lysine N-methyltransferase EEF2KMT; Catalyzes the trimethylation of eukaryotic elongation factor 2 (EEF2) on 'Lys-525'.	0.924
FAM86B1	FAM86B2	ENSP00000407067	ENSP00000262365	Putative protein N-methyltransferase FAM86B1; Family with sequence similarity 86 member B1.	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	0.948
FAM86B1	NPIPB8	ENSP00000407067	ENSP00000434399	Putative protein N-methyltransferase FAM86B1; Family with sequence similarity 86 member B1.	Nuclear pore complex interacting protein family member B8; Belongs to the NPIP family.	0.491
FAM86B1	SLC35G4	ENSP00000407067	ENSP00000490812	Putative protein N-methyltransferase FAM86B1; Family with sequence similarity 86 member B1.	Solute carrier family 35 member G4.	0.499
FAM86B2	C8orf48	ENSP00000262365	ENSP00000297324	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	Uncharacterized protein C8orf48; Chromosome 8 open reading frame 48.	0.470
FAM86B2	CCT3	ENSP00000262365	ENSP00000295688	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	T-complex protein 1 subunit gamma; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	0.467
FAM86B2	CCT4	ENSP00000262365	ENSP00000377958	Putative protein N-methyltransferase FAM86B2; Family with sequence similarity 86 member B2.	T-complex protein 1 subunit delta; Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. As part of the TRiC complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. The TRiC complex plays a role in the folding of actin and tubulin (Probable).	0.535